ArticleBiophysical chemistry2010
Band 3 catalyzes sickle hemoglobin polymerization.
Article in Biophysical chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- Article
- Metabolic correlates to critical speed in murine models of sickle cell disease.Frontiers in physiology · 2023Article
- Fluorescence assay of the interaction between hemoglobin and the cytoplasmic domain of erythrocyte membrane band 3.Blood cells, molecules & diseases · 2015Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
We have measured homogeneous and heterogeneous nucleation rates of sickle hemoglobin (HbS) in the presence of a strongly binding deletion mutant of the cytoplasmic domain of band 3 (cdb3), a membrane protein known to form dimers and to bind 2 HbS molecules to such a dimer, and we find that it accelerated both rates by a factor of 2. A weakly binding mutant, in contrast showed no impact on nucleation rates, contrary to naïve expectations of a slight enhancement based on the molecular crowding of the solution by the mutant. We find we can explain these phenomena by a model of HbS-cdb3 interaction in which the strong binding mutant, by stabilizing an HbS dimer, catalyzes the nucleation process, while the weak mutant binds only 1 HbS molecule, effectively inactivating it and thereby compensating for the crowding of the solution by the cdb3. The catalytic behavior we observe could play a role in intracellular processes.
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Registered trials
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